Article
Dynamics of a mobile loop at the active site of Escherichia coli asparaginase.
Biochimica et biophysica acta - 29 Sept 2000
Aung H P, Bocola M, Schleper S, Röhm K H
Abstract excerpt
Asparaginase II from Escherichia coli is well-known member of the bacterial class II amidohydrolases. Enzymes of this family utilize a peculiar catalytic mechanism in which a pair of threonine residues play pivotal roles. Another common feature is a mobile surface loop that closes over the active site when the substrates is bound. We have studied the motion of the loop by stopped-flow experiments using the...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.